A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Kohsaka, H., Takasu, E., Nose, A. (2007). In vivo induction of postsynaptic molecular assembly by the cell adhesion molecule Fasciclin2.  J. Cell Biol. 179(6): 1289--1300. (Export to RIS)
FlyBase ID FBrf0201824
Publication Type Research paper
PubMed ID 18070911
PubMed Abstract Cell adhesion molecules (CAMs) are thought to mediate interactions between innervating axons and their targets. However, such interactions have not been directly observed in vivo. In this paper, we study the function and dynamics of Fasciclin2 (Fas2), a homophilic CAM expressed both pre- and postsynaptically during neuromuscular synapse formation in Drosophila melanogaster. We apply live imaging of functional fluorescent fusion proteins expressed in muscles and find that Fas2 and Discs-Large (Dlg; a scaffolding protein known to bind Fas2) accumulate at the synaptic contact site soon after the arrival of the nerve. Genetic, deletion, and photobleaching analyses suggest that Fas2-mediated trans-synaptic adhesion is important for the postsynaptic accumulation of both Fas2 itself and Dlg. In fas2 mutants, many aspects of synapse formation appear normal; however, we see a reduction in the synaptic accumulation of Scribble (another scaffolding protein) and glutamate receptor subunits GluRIIA and GluRIIB. We propose that Fas2 mediates trans-synaptic adhesion, which contributes to postsynaptic molecular assembly at the onset of synaptogenesis.
DOI 10.1083/jcb.200705154
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Language of Publication English
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Publication Type Journal
Abbreviation J. Cell Biol.
Title Journal of Cell Biology
Publication Year 1966-
ISBN/ISSN 0021-9525
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